NCL_ARATH
ID NCL_ARATH Reviewed; 585 AA.
AC Q8L636; Q67ZY8; Q9ASV9; Q9MAH9;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sodium/calcium exchanger NCL {ECO:0000305};
DE AltName: Full=Na(+)/Ca(2+)-exchange protein NCL {ECO:0000305};
DE AltName: Full=Protein NCX-like {ECO:0000303|PubMed:23148213};
DE Short=AtNCL {ECO:0000303|PubMed:23148213};
GN Name=NCL {ECO:0000303|PubMed:23148213};
GN OrderedLocusNames=At1g53210 {ECO:0000312|Araport:AT1G53210};
GN ORFNames=F12M16.12 {ECO:0000312|EMBL:AAF69532.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 438-585.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23148213; DOI=10.1074/jbc.m112.351643;
RA Wang P., Li Z., Wei J., Zhao Z., Sun D., Cui S.;
RT "A Na+/Ca2+ exchanger-like protein (AtNCL) involved in salt stress in
RT Arabidopsis.";
RL J. Biol. Chem. 287:44062-44070(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26296956; DOI=10.1111/pce.12620;
RA Li P., Zhang G., Gonzales N., Guo Y., Hu H., Park S., Zhao J.;
RT "Ca(2+)-regulated and diurnal rhythm-regulated Na(+)/Ca(2+) exchanger AtNCL
RT affects flowering time and auxin signalling in Arabidopsis.";
RL Plant Cell Environ. 39:377-392(2016).
CC -!- FUNCTION: Possesses sodium/calcium exchanger (NCX) activity when
CC expressed in a heterologous mammalian CHO-K1 cell system
CC (PubMed:23148213). Does not possess cation/proton exchanger (CAX) or
CC sodium/proton (NHX) activity when expressed in a heterologous yeast
CC cell system. Has the ability to bind calcium in vitro. Participates in
CC the maintenance of calcium homeostasis (PubMed:23148213,
CC PubMed:26296956). May play a role in auxin response, diurnal rhythm and
CC flowering time (PubMed:26296956). Involved in salt stress response
CC (PubMed:23148213). {ECO:0000269|PubMed:23148213,
CC ECO:0000269|PubMed:26296956}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23148213};
CC Multi-pass membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:26296956}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, petals, stamens,
CC ovules and siliques. {ECO:0000269|PubMed:23148213}.
CC -!- INDUCTION: Induced by salt stress (PubMed:23148213, PubMed:26296956).
CC Induced by cold stress, heat shock and abscisic acid (ABA)
CC (PubMed:23148213). Induced by calcium and magnesium chloride, and
CC osmotic shock (PubMed:26296956). {ECO:0000269|PubMed:23148213,
CC ECO:0000269|PubMed:26296956}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:23148213). No visible phenotype under short day (SD)
CC conditions, but early flowering under long day (LD) conditions
CC (PubMed:26296956). {ECO:0000269|PubMed:23148213,
CC ECO:0000269|PubMed:26296956}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF69532.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008007; AAF69532.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32908.1; -; Genomic_DNA.
DR EMBL; AF361800; AAK32813.1; -; mRNA.
DR EMBL; AY099550; AAM20402.1; -; mRNA.
DR EMBL; AY133619; AAM91449.1; -; mRNA.
DR EMBL; AK175716; BAD43479.1; -; mRNA.
DR EMBL; AK176146; BAD43909.1; -; mRNA.
DR EMBL; AK175979; BAD43742.1; -; mRNA.
DR PIR; G96572; G96572.
DR RefSeq; NP_564623.2; NM_104200.3.
DR AlphaFoldDB; Q8L636; -.
DR STRING; 3702.AT1G53210.1; -.
DR iPTMnet; Q8L636; -.
DR PaxDb; Q8L636; -.
DR PRIDE; Q8L636; -.
DR ProteomicsDB; 251315; -.
DR EnsemblPlants; AT1G53210.1; AT1G53210.1; AT1G53210.
DR GeneID; 841755; -.
DR Gramene; AT1G53210.1; AT1G53210.1; AT1G53210.
DR KEGG; ath:AT1G53210; -.
DR Araport; AT1G53210; -.
DR TAIR; locus:2009580; AT1G53210.
DR eggNOG; ENOG502QV8Y; Eukaryota.
DR HOGENOM; CLU_023891_0_0_1; -.
DR InParanoid; Q8L636; -.
DR OMA; HTMKFLS; -.
DR OrthoDB; 435926at2759; -.
DR PhylomeDB; Q8L636; -.
DR PRO; PR:Q8L636; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L636; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:TAIR.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0071472; P:cellular response to salt stress; IMP:TAIR.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR004713; CaH_exchang.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR004837; NaCa_Exmemb.
DR PANTHER; PTHR31503; PTHR31503; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Antiport; Calcium; Calcium transport; Cell membrane; Glycoprotein;
KW Ion transport; Membrane; Metal-binding; Reference proteome; Repeat; Sodium;
KW Sodium transport; Stress response; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..585
FT /note="Sodium/calcium exchanger NCL"
FT /id="PRO_5009715792"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 299..334
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 339..374
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 585 AA; 63417 MW; F74FC67C4EB1EB96 CRC64;
MRFRSLISLL FLLFFTSSAY ARFVSLNPSS TSLISDGIDG GSNLAGSGSV IKSVVSAPAE
EKEEACEQTY GFMPCTKTAL GNVFLILVYG FLMFTAATYL SAGSELLLEI LGPGIVGGLF
LPMLGALPDA MLIMVSGLSG DAATAQSQVS VGMGLLAGST VMLLTVIWGT CTVVGKCDLR
DSIAVNNQDT KGFHLKDSGV TVDIWTSYAA RIMAISVIPF VIVQLPQMLG STSGRQLSVL
IALILSVLML ISYCVYQVFQ PWIQRRRLAF AKHKHVISGI LRHLKQHALG RLLDDEGQPD
EHVIRKLFLT IDANNDGHLS AAELKALIIG ISFEDIDFDK DDAVGKVLQD FDKTLDEQVD
QEEFVRGIKQ WLIQAMGGAP SGPEAGPRTM KFLDNFHVQT KREHALLGDN ENGENDEEGG
EVADPKWITI KAALLLLLGA AIAAAFADPL VDTVNNFSAA TGIPSFFISF IALPLATNSS
EAVSAIIFAS RKKIRTASLT FSELCGGVTM NNILCLSVFL AIVYVRGLTW NFSSEVLVIL
IVCLVMGGFA SFRTTYPLWT CFIAYLLYPF SLGLVYILDY WFGWS
